M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation

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dc.catalogadorpau
dc.contributor.authorReyes Valenzuela, Juan Sebastian
dc.contributor.authorFuentes-Lemus, Eduardo
dc.contributor.authorAspée, Alexis
dc.contributor.authorDavies, Michael J.
dc.contributor.authorMonasterio, Octavio
dc.contributor.authorLópez Alarcón, Camilo Ignacio
dc.date.accessioned2025-01-03T19:52:39Z
dc.date.available2025-01-03T19:52:39Z
dc.date.issued2021
dc.description.abstractOxidation and inactivation of FtsZ is of interest due to the key role of this protein in bacterial cell division. In the present work, we studied peroxyl radical (from AAPH, 2,2′-azobis(2-methylpropionamidine)dihydrochloride) mediated oxidation of the highly stable FtsZ protein (MjFtsZ) from M. jannaschii, a thermophilic microorganism. MjFtsZ contains eleven Met, and single Tyr and Trp residues which would be expected to be susceptible to oxidation. We hypothesized that exposure of MjFtsZ to AAPH-derived radicals would induce Met oxidation, and cross-linking (via di-Tyr and di-Trp formation), with concomitant loss of its functional polymerization and depolymerization (GTPase) activities. Solutions containing MjFtsZ and AAPH (10 or 100 mM) were incubated at 37 °C for 3 h. Polymerization/depolymerization were assessed by light scattering, while changes in mass were analyzed by SDS-PAGE. Amino acid consumption was quantified by HPLC with fluorescence detection, or direct fluorescence (Trp). Oxidation products and modifications at individual Met residues were quantified by UPLC with mass detection. Oxidation inhibited polymerization-depolymerization activity, and yielded low levels of irreversible protein dimers. With 10 mM AAPH only Trp and Met were consumed giving di-alcohols, kynurenine and di-Trp (from Trp) and the sulfoxide (from Met). With 100 mM AAPH low levels of Tyr oxidation (but not di-Tyr formation) were also observed. Correlation with the functional analyses indicates that Met oxidation, and particularly Met164 is the key driver of MjFtsZ inactivation, probably as a result of the position of this residue at the protein-protein interface of longitudinal interactions and in close proximity to the GTP binding site.
dc.fechaingreso.objetodigital2025-01-03
dc.format.extent13 páginas
dc.fuente.origenConveris
dc.identifier.converisid1
dc.identifier.doi10.1016/j.freeradbiomed.2021.02.003
dc.identifier.issn0891-5849
dc.identifier.scopusidScopus_ID:2-s2.0-85101347890
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/89515
dc.identifier.wosidWoS_Id: 000632701700005
dc.information.autorucEscuela de Química; Reyes Valenzuela, Juan Sebastian; S/I; 1268701
dc.information.autorucEscuela de Química; López Alarcón, Camilo Ignacio; S/I; 1004308
dc.language.isoen
dc.nota.accesocontenido parcial
dc.pagina.final66
dc.pagina.inicio53
dc.publisherElsevier
dc.revistaFree Radical Biology and Medicine
dc.rightsacceso restringido
dc.subjectThermophiles
dc.subjectFtsZ
dc.subjectMethanococcus jannaschii
dc.subjectAAPH
dc.subjectPeroxyl radicals
dc.subjectdi-tryptophan bonds
dc.subjectMethionine oxidation
dc.subject.ddc510
dc.subject.deweyMatemática física y químicaes_ES
dc.titleM. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation
dc.typeartículo
dc.volumen166
sipa.codpersvinculados1268701
sipa.codpersvinculados1004308
sipa.trazabilidadConveris;20-07-2021
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